Structural mass spectrometry (MS) is gaining increasing importance for deriving valuable three-dimensional structural information on proteins and protein complexes, and it complements existing techniques, such as NMR spectroscopy and X-ray crystallography. Structural MS unites different MS-based techniques, such as hydrogen/deuterium exchange, native MS, ion-mobility MS, protein footprinting, and chemical cross-linking/MS, and it allows fundamental questions in structural biology to be addressed.

"The Charles Tanford Protein Center (CTP) is a research building of Martin Luther University Halle-Wittenberg that is dedicated to protein research. The CTP houses groups from three different faculties: the Faculty of Natural Sciences I (seven groups from the Institute of Biochemistry and Biotechnology and one from the Institute of Pharmacy), the Faculty of Natural Sciences II (one group from the Institute of Chemistry) and the Medical Faculty (Institute of Molecular Medicine). The CTP also accommodates the interdisciplinary ZIK HALOmem, working on membrane proteins, as well as a central service facility for mass spectrometry and a core facility Imaging. Research topics at the CTP range from chemical to medical and biological problems and comprise, among others, the following topics: protein and peptide chemistry, protein structure, post-translational protein modifications, membrane proteins, roles of proteins in RNA metabolism and in tumor formation. Participating scientists use a number of sophisticated methods, including X-ray crystallography, NMR, mass spectrometry, high-end light microscopy, chemical peptide synthesis etc. Other equipment and methods, such as higher field NMR spectrometers, can be used in cooperation with neighboring institutions...".